Diaminopropionate ammonia-lyase (dpaL) Recombinant Protein | dpaL recombinant protein

Recombinant Salmonella typhimurium Diaminopropionate ammonia-lyase (dpaL)

Cat. Num. AAA1142695

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Diaminopropionate ammonia-lyase (dpaL); Recombinant Salmonella typhimurium Diaminopropionate ammonia-lyase (dpaL); dpaL recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-404, Full length protein
• Sequence: MHELIKYQFNTRRKKYGTGAALSLLNGNVGHEVLAFHKKLPNYAVTPLHNLAHLSQRLGLGSIHIKDESWRFGLNAFKGLGGSYAVGKYLADKLQCDINSLSFAALNTPEIKEKIKDCVFVTATDGNHGRGVAWAAEQLGLKAVVYMPKGSSLIRAENIRHHGAECTITDLNYDDAVRLAHRMAQTKGWVLLQDTAWTGYEEIPTWIMQGYMTLAVEAYEQLAETNSPLPTHLILQAGVGSFAGSVMGYFVEKMQENIPNIIVVEPHQANCLYQSAVMDDGQPHCVTGDMATIMAGLACGEPNIISWPIIRDNTSCFISADDCLAAKGMRISAAPRPGTDTPFISGESGAIGVGLLYELMNNMHYQDLANRLQLDASAHVLLISTEGDTSPDIYEDIVWNGRSA
• Sequence Length: 404

• Species: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

NCBI and Uniprot Product Information

• NCBI GI #: 16764362
• NCBI GeneID: 1252520
• NCBI Accession #: NP_459977.1
• NCBI GenBank Nucleotide #: NC_003197.2
• UniProt Accession #: P40817
• Molecular Weight: 44,152 Da
• NCBI Official Full Name: diaminopropionate ammonia-lyase
• NCBI Official Symbol: STM1002
• NCBI Protein Information: diaminopropionate ammonia-lyase
• UniProt Protein Name: Diaminopropionate ammonia-lyase
• UniProt Gene Name: dpaL
• UniProt Synonym Gene Names: DAPAL

Uniprot Description

Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them.